Discovery of structural and functional transition sites for membrane-penetrating activity of sheep myeloid antimicrobial peptide-18.

ABSTRACT: Cathelicidin antimicrobial peptides have an extended and/or unstructured conformation in aqueous solutions but fold into ordered conformations, such as the α-helical structure, when interacting with cellular membranes. These structural transitions can be directly correlated to their antimicrobial activity and its underlying mechanisms. SMAP-18, the N-terminal segment (residues 1-18) of sheep cathelicidin (SMAP-29), is known to kill microorganisms by translocating across membranes and interacting with their nucleic acids. The amino acid sequence of SMAP-18 contains three Gly residues (at positions 2, 7, and 13) that significantly affect the flexibility of its peptide structure. This study investigated the role of Gly residues in the structure, membrane interaction, membrane translocation, a

SUBMITTER: Jung B 

PROVIDER: S-EPMC9871035 | biostudies-literature | 2023 Jan

REPOSITORIES: biostudies-literature